The epidermal growth factor receptor associates with and recruits phosphatidylinositol 3-kinase to the platelet-derived growth factor beta receptor

摘要: Receptor tyrosine kinases are classified into subfamilies, which believed to function independently, with heterodimerization occurring only within the same subfamily. In this study, we present evidence suggesting a direct interaction between epidermal growth factor (EGF) receptor (EGFR) and platelet-derived beta (PDGFbeta) (PDGFbetaR), members of different kinase subfamilies. We find that addition EGF COS-7 cells human foreskin Hs27 fibroblasts results in rapid phosphorylation PDGFbetaR recruitment phosphatidylinositol 3-kinase PDGFbetaR. R1hER cells, overexpress EGFR, ligand-independent constitutive binding substantial amount PI-3 activity it, mimicking effect ligand untransfected cells. support possibility may be interaction, show two receptors can coimmunoprecipitated from This association reconstituted by introducing 293 EBNA The EGFR/PDGFbetaR is all cell lines tested. also demonstrate fraction bound EGFR undergoes an EGF-induced mobility shift on Western blots indicative phosphorylation. Our findings indicate interactions under subfamilies more widespread than previously believed.